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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2008-10-20
pubmed:abstractText
Flavonoids are polyphenolic compounds that are ubiquitous in nature. They possess varied promising properties for medical use. Quercetin (3,3',4',5,7-pentahydroxyflavone) and apigenin (4',5,7-trihydroxyflavone) are two representative flavonoids, both of which have been reported to possess antibacterial activity by acting on multiple targets. Here, we determined that d-alanine:d-alanine ligase (Ddl) is another new target for quercetin and apigenin. Kinetic analysis indicated that these two flavonoids function as reversible inhibitors that are competitive with the substrate ATP of Ddl, whereas they are non-competitive with the other substrate d-Ala. The fact that quercetin showed lower 50% inhibitory concentration (IC(50)) and inhibitor binding constant (K(i)) values than apigenin against both the Helicobacter pylori Ddl and the Escherichia coli DdlB implies that the two additional hydroxyls on the flavone skeleton of quercetin in structure might facilitate its inhibitory activity and binding affinity to Ddl. This work is expected to help shed more light on the potential antibacterial mechanism of flavonoids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0924-8579
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-6
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
D-Alanine:D-alanine ligase as a new target for the flavonoids quercetin and apigenin.
pubmed:affiliation
Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't